The mechanism by which long chain fatty acyl CoA esters bind to the adenine nucleotide translocase, thereby producing inihibition of transport, will be studied. An effort will be made to reverse the inihibition, particularly in the ischemic myocardium, by the use of appropriate physiological and pharmacological agents. To determine the intracellular concentration and compartmentation of the adenine and pyridine nucleotides as well as long chain acyl CoA esters. The amino acid sequence and various physical and chemical parameters of the homogenous ATPase isolated from Tetrahymena pyriformis will be carried out. An antibody to the pure protein hs been obtained to better locate the intracellular site of the enzyme as well as its presence in other organisms. BIBLIOGRAPHIC REFERENCES: Sul, H.S., Shrago, E. and Shug, A.L. (1976) Relationship of Phosphoenolpyruvate Transport, Acyl Co-enzyme A Inihibition of Adenine Nucleotide Translocase and Calcium Ion Efflux in Guinea Pig Heart Mitochondria. Arch. Biochem. Biophys. 172: 230-237. Shrago, E., Shug, A. and Elson, C. (1976) Regulation of Cell Metabolism by Mitochondrial Transport Systems. In: Gluconeogenesis (R.W. Hanson and M.A. Mehlman, eds.) John Wiley and Sons, New York, pp. 221-238.